The disclosure relates, in general, to evaluating peptide synthesis and, more particularly, to a system and method for identifying and implementing quality control oligopeptide sequences for assaying longitudinal peptide synthesis fidelity.
Peptides are biological polymers assembled, in part, through the formation of amide bonds between amino acid monomer units. In general, peptides may be distinguished from their protein counterparts based on factors such as size (e.g., number of monomer units or molecular weight), complexity (e.g., number of peptides, presence of coenzymes, cofactors, or other ligands), and the like. Experimental approaches for the identification of binding motifs, epitopes, mimotopes, disease markers, or the like may successfully employ peptides instead of larger or more complex proteins that may be more difficult to obtain or manipulate. As a result, the study of peptides and the capability to synthesize those peptides are of significant interest in the biological sciences and medicine.
Several methods exist for the synthesis of peptides including both in vivo and in vitro translation systems, as well as organic synthesis routes such as solid phase peptide synthesis. Solid phase peptide synthesis is a technique in which an initial amino acid is linked to a solid surface such as a bead, a microscope slide, or another like surface. Thereafter, subsequent amino acids are added in a step-wise manner to the initial amino acid to form a peptide chain. Because the peptide chain is attached to a solid surface, operations such as wash steps, side chain modifications, cyclization, or other treatment steps may be performed with the peptide chain maintained in a discrete location.
Recent advances in solid phase peptide synthesis have led to automated synthesis platforms for the parallel assembly of millions of unique peptide features in an array on a single surface (e.g., a ˜75 mm×˜25 mm microscope slide). The utility of such peptide arrays is, at least in part, dependent on the accuracy and fidelity with which the synthesis is carried out. For example, if the reagents used for synthesis are degraded, contaminated or improperly transported to the array surface during synthesis, a given peptide feature may have an altered, incomplete, or truncated peptide sequence. Other errors in peptide synthesis may also occur. However, it is generally impractical with currently available technologies to assay the quality of every individual feature on a routine basis due to both the number of features synthesized on a given array, and the associated material mass synthesized for each feature.
Accordingly, there is a need for improved processes and systems for the analysis of synthesis fidelity for peptide arrays as well as for peptide synthesis in general.